MIR Is a Novel ERM-like Protein That Interacts with Myosin Regulatory Light Chain and Inhibits Neurite Outgrowth
Open accessAbstract
The ERM protein family members ezrin, radixin, and moesin are cytoskeletal effector proteins linking actin to membrane-bound proteins at the cell surface. Here we report on the cloning of myosin regulatory light chain interacting protein (MIR), a protein with an ERM-homology domain and a carboxyl-terminal RING finger, that is expressed, among other tissues, in brain. MIR is distributed in cultured COS cells, in a punctuated manner as shown using enhanced green fluorescent protein (EGFP)-tagged MIR and by staining with a specific antibody for MIR. In the yeast two-hybrid system and in transfected COS cells, MIR interacts with myosin regulatory light chain B, which in turn regulates the activity of the actomyosin complex. Overexpression of MIR cDNA in PC12 cells abrogated neurite outgrowth induced by nerve growth factor (NGF) without affecting TrkA signaling. The results show that MIR, a novel ERM-like protein, affects cytoskeleton interactions regulating cell motility, such as neurite outgrowth.
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IDOL is a unique ERM family member in that it contains a RING unit in addition to the signature FERM domain.
“IDOL is a unique ERM family member in that it contains a RING unit in addition to the signature FERM domain (10,21).”
From Distinct Functional Domains Contribute to Degradation of the Low Density Lipoprotein Receptor (LDLR) by the E3 Ubiquitin Ligase Inducible Degrader of the LDLR (IDOL) (2011) · cites this paper as [10]
The Discussion (page unavailable) describes MIR as a novel ERM-family protein with an amino-terminal ERM-homology domain and a carboxyl-terminal RING finger. Our copy does not identify MIR as IDOL, so it does not establish that the stated domain combination belongs to the protein named in the claim. (LLM, conf=0.78)
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Research works printed but not linked: 1
- Wylie, S. R., Wu, P.-J., Patel, H., and Chantler, P. D. (1998) Proc. Natl. Acad. Sci. U. S. A. 95, 12967-12972
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- Authors
- Olsson, P.-A., Korhonen, L., Mercer, E. A., & Lindholm, D.
- Affiliations
- Uppsala University (SE)
- Corresponding author
- Lindholm, Dan
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1999-12
- Volume
- 274
- Issue
- 51
- Pages
- 36288-36292
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1976896971
- Cited by
- 77
- References
- 0
- Citations by year
- 2026: 2 · 2025: 1 · 2024: 3 · 2023: 1 · 2022: 2 · 2021: 3 · 2020: 1 · 2019: 2 · 2018: 4 · 2017: 1 · 2016: 3 · 2015: 4 · 2014: 5 · 2013: 6 · 2012: 6
- FWCI
- 0.82
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Swedish Cancer Foundation
- Cancerfonden
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Axon Guidance and Neuronal Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- ERM proteins, ezrin, radixin, moesin, ring finger, actomyosin, neurite outgrowth, nerve growth factor, TrkA signaling, cytoskeleton, cell motility, PC12 cells, brain
- MeSH terms
- Amino Acid Sequence, Animals, Carrier Proteins, Cell Differentiation, Cloning, Molecular, Humans, Molecular Sequence Data, Nerve Tissue Proteins, Neurons, Sequence Alignment, Neurites, PC12 Cells, DNA, Complementary, Myosin Light Chains, Ubiquitin-Protein Ligases, Rats
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